5VCW

CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Pelitinib

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2014-08-25
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.00
Spacegroup name	P 1 21 1
Unit cell lengths	50.510, 112.900, 72.710
Unit cell angles	90.00, 109.27, 90.00

Refinement procedure

Resolution	36.425 - 2.250
Rwork	0.196
R-free	0.24570
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5vcv
RMSD bond length	0.010
RMSD bond angle	1.235
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	36.425	36.425	2.310
High resolution limit [Å]	2.250	10.060	2.250
Rmerge	0.076	0.075	0.302
Rmeas	0.091	0.090	0.357
Number of reflections	36183	396	2679
<I/σ(I)>	10.29	16.89	3.85
Completeness [%]	98.9	92.7	99.4
Redundancy	3.426	3.235	3.425
CC(1/2)	0.992	0.989	0.950

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291	6.9 MG/ML MYT1, 25 mM HEPES, 100 MM SODIUM CHLORIDE, 0.5 mM DTT, 0.05 M MES pH 6.5, 0.8 M Magnesium sulfate, 2 mM Pelitinib